caa a22 4500 445325321 CHVBK 20180317142718.0 cr unu---uuuuu 170323e20111201xx s 000 0 eng 10.1007/s10858-011-9579-0 doi (NATIONALLICENCE)springer-10.1007/s10858-011-9579-0 Uncovering symmetry-breaking vector and reliability order for assigning secondary structures of proteins from atomic NMR chemical shifts in amino acids [Elektronische Daten] [Wookyung Yu, Woonghee Lee, Weontae Lee, Suhkmann Kim, Iksoo Chang] Unravelling the complex correlation between chemical shifts of 13 C α,13 C β,13 C′,1 H α,15 N,1 H N atoms in amino acids of proteins from NMR experiment and local structural environments of amino acids facilitates the assignment of secondary structures of proteins. This is an important impetus for both determining the three-dimensional structure and understanding the biological function of proteins. The previous empirical correlation scores which relate chemical shifts of 13 C α,13 C β,13 C′,1 H α,15 N,1 H N atoms to secondary structures resulted in progresses toward assigning secondary structures of proteins. However, the physical-mathematical framework for these was elusive partly due to both the limited and orthogonal exploration of higher-dimensional chemical shifts of hetero-nucleus and the lack of physical-mathematical understanding underlying those correlation scores. Here we present a simple multi-dimensional hetero-nuclear chemical shift score function (MDHN-CSSF) which captures systematically the salient feature of such complex correlations without any references to a random coil state of proteins. We uncover the symmetry-breaking vector and its reliability order not only for distinguishing different secondary structures of proteins but also for capturing the delicate sensitivity interplayed among chemical shifts of 13 C α,13 C β,13 C′,1 H α,15 N,1 H N atoms simultaneously, which then provides a straightforward framework toward assigning secondary structures of proteins. MDHN-CSSF could correctly assign secondary structures of training (validating) proteins with the favourable (comparable) Q3 scores in comparison with those from the previous correlation scores. MDHN-CSSF provides a simple and robust strategy for the systematic assignment of secondary structures of proteins and would facilitate the de novo determination of three-dimensional structures of proteins. Springer Science+Business Media B.V., 2011 Assigning secondary structures of proteins nationallicence NMR chemical shift nationallicence Complex correlation between chemical shifts and secondary structures of proteins nationallicence Singular value decomposition analysis nationallicence Yu Wookyung Department of Physics, Center for Proteome Biophysics, Pusan National University, 609-735, Busan, Korea aut Lee Woonghee Department of Biochemistry, Structural Biochemistry and Molecular Biophysics Laboratory, Yonsei University, 120-749, Seoul, Korea aut Lee Weontae Department of Biochemistry, Structural Biochemistry and Molecular Biophysics Laboratory, Yonsei University, 120-749, Seoul, Korea aut Kim Suhkmann Department of Chemistry, Biochemistry and Bio-NMR Laboratory, Pusan National University, 609-735, Busan, Korea aut Chang Iksoo Department of Physics, Center for Proteome Biophysics, Pusan National University, 609-735, Busan, Korea aut Journal of Biomolecular NMR Springer Netherlands 51/4(2011-12-01), 411-424 0925-2738 51:4<411 2011 51 10858 https://doi.org/10.1007/s10858-011-9579-0 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9579-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Yu Wookyung Department of Physics, Center for Proteome Biophysics, Pusan National University, 609-735, Busan, Korea aut NATIONALLICENCE 700 1- Lee Woonghee Department of Biochemistry, Structural Biochemistry and Molecular Biophysics Laboratory, Yonsei University, 120-749, Seoul, Korea aut NATIONALLICENCE 700 1- Lee Weontae Department of Biochemistry, Structural Biochemistry and Molecular Biophysics Laboratory, Yonsei University, 120-749, Seoul, Korea aut NATIONALLICENCE 700 1- Kim Suhkmann Department of Chemistry, Biochemistry and Bio-NMR Laboratory, Pusan National University, 609-735, Busan, Korea aut NATIONALLICENCE 700 1- Chang Iksoo Department of Physics, Center for Proteome Biophysics, Pusan National University, 609-735, Busan, Korea aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/4(2011-12-01), 411-424 0925-2738 51:4<411 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer